This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Among the phospholipases A2 (PLA2s) are the Group VI Ca2+-independent PLA2s (iPLA2s) andexpression of multiple transcripts of iPLA2 in skeletal muscle has been reported. In the present study, lipaseactivity and sequential ATP and calmodulin affinity column chromatography analyses reveal that skeletal muscleiPLA2 exhibits properties characteristic of the iPLA2[unreadable] isoform. The lipase activity of iPLA2[unreadable] has been demonstrated to participate in phospholipid remodeling, signal transduction, cell proliferation, and apoptosis.